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Database: UniProt
Entry: W4PZL8_9BACI
LinkDB: W4PZL8_9BACI
Original site: W4PZL8_9BACI 
ID   W4PZL8_9BACI            Unreviewed;       246 AA.
AC   W4PZL8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:GAE24549.1};
GN   ORFNames=JCM9140_486 {ECO:0000313|EMBL:GAE24549.1};
OS   Halalkalibacter wakoensis JCM 9140.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX   NCBI_TaxID=1236970 {ECO:0000313|EMBL:GAE24549.1, ECO:0000313|Proteomes:UP000018890};
RN   [1] {ECO:0000313|EMBL:GAE24549.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 9140 {ECO:0000313|EMBL:GAE24549.1};
RA   Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequences of Three Alkaliphilic Bacillus Strains, Bacillus
RT   wakoensis JCM 9140T, Bacillus akibai JCM 9157T, and Bacillus
RT   hemicellulosilyticus JCM 9152T.";
RL   Genome Announc. 2:e01258-13(2014).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       ECO:0000256|RuleBase:RU003719}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAE24549.1}.
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DR   EMBL; BAUT01000002; GAE24549.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4PZL8; -.
DR   STRING; 1236970.JCM9140_486; -.
DR   Proteomes; UP000018890; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   CDD; cd05301; GDH; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR10996:SF178; GLYOXYLATE REDUCTASE 1; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018890}.
FT   DOMAIN          2..240
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          29..208
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   246 AA;  27177 MW;  70FBD5C4860258F2 CRC64;
     MDVAELTKRN IMATNTPGIL DDTTADAIFG LMLSTARRIP ELNQFVKDGK WNISLQPDQY
     GVDVHHKTLG IIGMGNIGSA IAKRANLGFG MNILYHNRSR NKQAEEAYQA IYCDLDELLE
     QSDFVCLMVP ATKETEKLMG ERQFKKMKNT AIFINGSRGK NVDEDALYDA LQNKDILAAG
     IDVFTEEPTN PKNPLLSLKN IVTLPHIGSS TTECEYNMSK LAADNLKSGL KGEKPPSIIN
     PEIFGN
//
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